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Influence of 2-mercaptoethanol on heat stability of concentrated whey-protein-free milk and formation of soluble casein

Takayoshi Aoki, Yoshitaka Kako

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Abstract

Summary The heat coagulation time (HCT) of concentrated whey-protein-free (WPF) milk measured at 120 and 130 °C was reduced to by addition of 5–20 mM-2-mercaptoethanol (ME). However, although the amount of soluble casein formed on heating was doubled by addition of ME, the shape of the HCT–pH profile was affected only slightly. The proportion of κ-casein in the soluble casein from heated concentrated WPF milk containing ME was very high, though it was somewhat lower than that of the soluble casein from heated concentrated WPF milk containing no ME. No solubilization of colloidal Ca phosphate was observed in either unheated or heated concentrated WPF milk on addition of ME. These facts suggest that ME probably promotes the formation of soluble casein with release of κ-casein from micelles on heating, thus destabilizing the casein micelles.

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Summary The heat coagulation time (HCT) of concentrated whey-protein-free (WPF) milk measured at 120 and 130 °C was reduced to by addition of 5–20 mM-2-mercaptoethanol (ME). However, although the amount of soluble casein formed on heating was doubled by addition of ME, the shape of the HCT–pH profile was affected only slightly. The proportion of κ-casein in the soluble casein from heated concentrated WPF milk containing ME was very high, though it was somewhat lower than that of the soluble casein from heated concentrated WPF milk containing no ME. No solubilization of colloidal Ca phosphate was observed in either unheated or heated concentrated WPF milk on addition of ME. These facts suggest that ME probably promotes the formation of soluble casein with release of κ-casein from micelles on heating, thus destabilizing the casein micelles.

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Available abstract

Summary The heat coagulation time (HCT) of concentrated whey-protein-free (WPF) milk measured at 120 and 130 °C was reduced to by addition of 5–20 mM-2-mercaptoethanol (ME). However, although the amount of soluble casein formed on heating was doubled by addition of ME, the shape of the HCT–pH profile was affected only slightly. The proportion of κ-casein in the soluble casein from heated concentrated WPF milk containing ME was very high, though it was somewhat lower than that of the soluble casein from heated concentrated WPF milk containing no ME. No solubilization of colloidal Ca phosphate was observed in either unheated or heated concentrated WPF milk on addition of ME. These facts suggest that ME probably promotes the formation of soluble casein with release of κ-casein from micelles on heating, thus destabilizing the casein micelles.

Key concepts: Casein, Chemistry, Heat stability, Food science, Whey protein, Chromatography, Micelle, Phosphate

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